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Role of Inter-domain Cavity in the Attachment of the Orange Carotenoid Protein to the Phycobilisome Core and to the Fluorescence Recovery Proteinстатья
Информация о цитировании статьи получена из
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 16 февраля 2016 г.
- Авторы: Zlenko Dmitry V., Krasilnikov Pavel M., Stadnichuk Igor N.
- Журнал: Journal of Biomolecular Structure and Dynamics
- Том: 34
- Номер: 3
- Год издания: 2015
- Издательство: Adenine Press
- Местоположение издательства: United States
- Первая страница: 486
- Последняя страница: 496
- DOI: 10.1080/07391102.2015.1042913
- Аннотация: Using molecular modeling and known spatial structure of proteins, we have derived a universal 3D model of the orange carotenoid protein (OCP) and phycobilisome (PBS) interaction in the process of non-photochemical PBS quenching. The characteristic tip of the phycobilin domain of the core-membrane linker polypeptide (LCM) forms the attachment site on the PBS core surface for interaction with the central inter-domain cavity of the OCP molecule. This spatial arrangement has to be the most advantageous one because the LCM, as the major terminal PBS-fluorescence emitter, accumulates energy from the most other phycobiliproteins within the PBS before quenching by OCP. In agreement with the constructed model, in cyanobacteria, the small fluorescence recovery protein is wedged in the OCP’s central cavity, weakening the PBS and OCP interaction. The presence of another one protein, the red carotenoid protein, in some cyanobacterial species, which also can interact with the PBS, also corresponds to this model.
- Добавил в систему: Красильников Павел Михайлович
Прикрепленные файлы
| № | Имя | Описание | Имя файла | Размер | Добавлен |
|---|---|---|---|---|---|
| 1. | Полный текст | J_Biomol_Struct_Dyn_2015_Zlenko.pdf | 935,0 КБ | 3 октября 2015 [Pavel_M] |